<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Yang K</submitter><funding>Zhejiang Natural Science Foundation</funding><funding>National Natural Science Foundation of China</funding><pagination>6699</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC10537072</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>28(18)</volume><pubmed_abstract>Catechols have important applications in the pharmaceutical, food, cosmetic, and functional material industries. 4-hydroxyphenylacetate-3-hydroxylase (4HPA3H), a two-component enzyme system comprising HpaB (monooxygenase) and HpaC (FAD oxidoreductase), demonstrates significant potential for catechol production because it can be easily expressed, is highly active, and exhibits &lt;i>ortho&lt;/i>-hydroxylation activity toward a broad spectrum of phenol substrates. HpaB determines the &lt;i>ortho&lt;/i>-hydroxylation efficiency and substrate spectrum of the enzyme; therefore, studying its structure-activity relationship, improving its properties, and developing a robust HpaB-conducting system are of significance and value; indeed, considerable efforts have been made in these areas in recent decades. Here</pubmed_abstract><journal>Molecules (Basel, Switzerland)</journal><pubmed_title>Advances in 4-Hydroxyphenylacetate-3-hydroxylase Monooxygenase.</pubmed_title><pmcid>PMC10537072</pmcid><funding_grant_id>LY23B060001</funding_grant_id><funding_grant_id>32071268</funding_grant_id><funding_grant_id>32071268, 31971372</funding_grant_id><funding_grant_id>31971372</funding_grant_id><funding_grant_id>LY21B060003</funding_grant_id><funding_grant_id>32371542</funding_grant_id><funding_grant_id>LY21B060003, LY23B060001</funding_grant_id><pubmed_authors>Mei L</pubmed_authors><pubmed_authors>Hu S</pubmed_authors><pubmed_authors>Yang K</pubmed_authors><pubmed_authors>Huang J</pubmed_authors><pubmed_authors>Mei J</pubmed_authors><pubmed_authors>Zhao W</pubmed_authors><pubmed_authors>Lv C</pubmed_authors><pubmed_authors>Zhang Q</pubmed_authors></additional><is_claimable>false</is_claimable><name>Advances in 4-Hydroxyphenylacetate-3-hydroxylase Monooxygenase.</name><description>Catechols have important applications in the pharmaceutical, food, cosmetic, and functional material industries. 4-hydroxyphenylacetate-3-hydroxylase (4HPA3H), a two-component enzyme system comprising HpaB (monooxygenase) and HpaC (FAD oxidoreductase), demonstrates significant potential for catechol production because it can be easily expressed, is highly active, and exhibits &lt;i>ortho&lt;/i>-hydroxylation activity toward a broad spectrum of phenol substrates. HpaB determines the &lt;i>ortho&lt;/i>-hydroxylation efficiency and substrate spectrum of the enzyme; therefore, studying its structure-activity relationship, improving its properties, and developing a robust HpaB-conducting system are of significance and value; indeed, considerable efforts have been made in these areas in recent decades. Here</description><dates><release>2023-01-01T00:00:00Z</release><publication>2023 Sep</publication><modification>2026-04-08T14:31:43.641Z</modification><creation>2025-02-19T00:00:46.168Z</creation></dates><accession>S-EPMC10537072</accession><cross_references><pubmed>37764475</pubmed><doi>10.3390/molecules28186699</doi></cross_references></HashMap>